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6M3C

hAPC-h1573 Fab complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0005509molecular_functioncalcium ion binding
D0005576cellular_componentextracellular region
G0004252molecular_functionserine-type endopeptidase activity
G0006508biological_processproteolysis
I0005509molecular_functioncalcium ion binding
I0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiDgigsFsCdC
ChainResidueDetails
BCYS111-CYS122

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EciEEiCdfeeakEifqnvddtla.FW
ChainResidueDetails
BGLU58-TRP83

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CdCrsGweGRfC
ChainResidueDetails
BCYS120-CYS131

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU249-CYS254

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPMV
ChainResidueDetails
AASP396-VAL407

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR196-HIS202
HTYR199-HIS205

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CdCrsGWegrf....C
ChainResidueDetails
BCYS120-CYS131
BCYS160-CYS175

site_idPS01187
Number of Residues33
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQClvlplehpcaslc.Cghgt...CiDgigsFsC
ChainResidueDetails
BASP88-CYS120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues714
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2991887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"2991887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"PubMed","id":"1694179","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2991887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues120
DetailsDomain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

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PDB entries from 2025-10-29

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